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Q99497

- PARK7_HUMAN

UniProt

Q99497 - PARK7_HUMAN

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Protein

Protein DJ-1

Gene

PARK7

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Protects cells against oxidative stress and cell death. Plays a role in regulating expression or stability of the mitochondrial uncoupling proteins SLC25A14 and SLC25A27 in dopaminergic neurons of the substantia nigra pars compacta and attenuates the oxidative stress induced by calcium entry into the neurons via L-type channels during pacemaking. Eliminates hydrogen peroxide and protects cells against hydrogen peroxide-induced cell death. Following removal of a C-terminal peptide, displays protease activity and enhanced cytoprotective action against oxidative stress-induced apoptosis. Stabilizes NFE2L2 by preventing its association with KEAP1 and its subsequent ubiquitination. Binds to OTUD7B and inhibits its deubiquitinating activity. Enhances RELA nuclear translocation. Binds to a number of mRNAs containing multiple copies of GG or CC motifs and partially inhibits their translation but dissociates following oxidative stress. Required for correct mitochondrial morphology and function and for autophagy of dysfunctional mitochondria. Regulates astrocyte inflammatory responses. Acts as a positive regulator of androgen receptor-dependent transcription. Prevents aggregation of SNCA. Plays a role in fertilization. Has no proteolytic activity. Has cell-growth promoting activity and transforming activity. May function as a redox-sensitive chaperone. May regulate lipid rafts-dependent endocytosis in astrocytes and neuronal cells.15 Publications

Kineticsi

  1. KM=173.4 µM for casein1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei106 – 10611 Publication
Active sitei126 – 12611 Publication

GO - Molecular functioni

  1. androgen receptor binding Source: ParkinsonsUK-UCL
  2. cupric ion binding Source: ParkinsonsUK-UCL
  3. cuprous ion binding Source: ParkinsonsUK-UCL
  4. cytokine binding Source: ParkinsonsUK-UCL
  5. enzyme binding Source: ParkinsonsUK-UCL
  6. glyoxalase (glycolic acid-forming) activity Source: ParkinsonsUK-UCL
  7. glyoxalase III activity Source: ParkinsonsUK-UCL
  8. identical protein binding Source: ParkinsonsUK-UCL
  9. L-dopa decarboxylase activator activity Source: ParkinsonsUK-UCL
  10. mRNA binding Source: UniProtKB
  11. oxidoreductase activity, acting on peroxide as acceptor Source: ParkinsonsUK-UCL
  12. peptidase activity Source: UniProtKB
  13. peroxidase activity Source: Ensembl
  14. peroxiredoxin activity Source: Ensembl
  15. protein homodimerization activity Source: UniProtKB
  16. receptor binding Source: UniProtKB
  17. repressing transcription factor binding Source: ParkinsonsUK-UCL
  18. RNA binding Source: ParkinsonsUK-UCL
  19. scaffold protein binding Source: ParkinsonsUK-UCL
  20. small protein activating enzyme binding Source: ParkinsonsUK-UCL
  21. small protein conjugating enzyme binding Source: ParkinsonsUK-UCL
  22. superoxide dismutase copper chaperone activity Source: ParkinsonsUK-UCL
  23. transcription coactivator activity Source: ParkinsonsUK-UCL
  24. transcription factor binding Source: ParkinsonsUK-UCL
  25. tyrosine 3-monooxygenase activator activity Source: ParkinsonsUK-UCL
  26. ubiquitin-specific protease binding Source: ParkinsonsUK-UCL

GO - Biological processi

  1. adult locomotory behavior Source: Ensembl
  2. autophagy Source: UniProtKB-KW
  3. cellular response to glyoxal Source: ParkinsonsUK-UCL
  4. cellular response to hydrogen peroxide Source: UniProtKB
  5. cellular response to oxidative stress Source: ParkinsonsUK-UCL
  6. dopamine uptake involved in synaptic transmission Source: Ensembl
  7. glycolate biosynthetic process Source: ParkinsonsUK-UCL
  8. glyoxal catabolic process Source: ParkinsonsUK-UCL
  9. hydrogen peroxide metabolic process Source: ParkinsonsUK-UCL
  10. inflammatory response Source: UniProtKB-KW
  11. lactate biosynthetic process Source: GOC
  12. membrane depolarization Source: Ensembl
  13. membrane hyperpolarization Source: Ensembl
  14. methylglyoxal catabolic process to D-lactate Source: ParkinsonsUK-UCL
  15. mitochondrion organization Source: UniProtKB
  16. negative regulation of apoptotic process Source: ParkinsonsUK-UCL
  17. negative regulation of cell death Source: UniProtKB
  18. negative regulation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway Source: ParkinsonsUK-UCL
  19. negative regulation of death-inducing signaling complex assembly Source: ParkinsonsUK-UCL
  20. negative regulation of extrinsic apoptotic signaling pathway Source: UniProtKB
  21. negative regulation of gene expression Source: ParkinsonsUK-UCL
  22. negative regulation of hydrogen peroxide-induced cell death Source: ParkinsonsUK-UCL
  23. negative regulation of hydrogen peroxide-induced neuron death Source: ParkinsonsUK-UCL
  24. negative regulation of neuron apoptotic process Source: BHF-UCL
  25. negative regulation of neuron death Source: ParkinsonsUK-UCL
  26. negative regulation of oxidative stress-induced cell death Source: ParkinsonsUK-UCL
  27. negative regulation of oxidative stress-induced neuron intrinsic apoptotic signaling pathway Source: ParkinsonsUK-UCL
  28. negative regulation of protein acetylation Source: ParkinsonsUK-UCL
  29. negative regulation of protein binding Source: UniProtKB
  30. negative regulation of protein export from nucleus Source: ParkinsonsUK-UCL
  31. negative regulation of protein K48-linked deubiquitination Source: ParkinsonsUK-UCL
  32. negative regulation of protein kinase activity Source: ParkinsonsUK-UCL
  33. negative regulation of protein phosphorylation Source: ParkinsonsUK-UCL
  34. negative regulation of protein sumoylation Source: ParkinsonsUK-UCL
  35. negative regulation of protein ubiquitination Source: ParkinsonsUK-UCL
  36. negative regulation of TRAIL-activated apoptotic signaling pathway Source: ParkinsonsUK-UCL
  37. negative regulation of ubiquitin-protein transferase activity Source: ParkinsonsUK-UCL
  38. negative regulation of ubiquitin-specific protease activity Source: ParkinsonsUK-UCL
  39. positive regulation of androgen receptor activity Source: ParkinsonsUK-UCL
  40. positive regulation of dopamine biosynthetic process Source: ParkinsonsUK-UCL
  41. positive regulation of interleukin-8 production Source: ParkinsonsUK-UCL
  42. positive regulation of L-dopa biosynthetic process Source: ParkinsonsUK-UCL
  43. positive regulation of L-dopa decarboxylase activity Source: ParkinsonsUK-UCL
  44. positive regulation of mitochondrial electron transport, NADH to ubiquinone Source: ParkinsonsUK-UCL
  45. positive regulation of oxidative phosphorylation uncoupler activity Source: Ensembl
  46. positive regulation of protein homodimerization activity Source: ParkinsonsUK-UCL
  47. positive regulation of protein localization to nucleus Source: ParkinsonsUK-UCL
  48. positive regulation of pyrroline-5-carboxylate reductase activity Source: ParkinsonsUK-UCL
  49. positive regulation of superoxide dismutase activity Source: ParkinsonsUK-UCL
  50. positive regulation of transcription from RNA polymerase II promoter Source: ParkinsonsUK-UCL
  51. positive regulation of tyrosine 3-monooxygenase activity Source: ParkinsonsUK-UCL
  52. protein stabilization Source: UniProtKB
  53. regulation of androgen receptor signaling pathway Source: UniProtKB
  54. regulation of fibril organization Source: ParkinsonsUK-UCL
  55. regulation of inflammatory response Source: UniProtKB
  56. regulation of mitochondrial membrane potential Source: ParkinsonsUK-UCL
  57. regulation of neuron apoptotic process Source: UniProtKB
  58. single fertilization Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chaperone, Hydrolase, Protease

Keywords - Biological processi

Autophagy, Fertilization, Inflammatory response, Stress response

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

SignaLinkiQ99497.

Protein family/group databases

MEROPSiC56.002.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein DJ-1 (EC:3.4.-.-)
Alternative name(s):
Oncogene DJ1
Parkinson disease protein 7
Gene namesi
Name:PARK7
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:16369. PARK7.

Subcellular locationi

Cell membrane; Lipid-anchor. Cytoplasm. Nucleus. Membrane raft. Mitochondrion
Note: Under normal conditions, located predominantly in the cytoplasm and, to a lesser extent, in the nucleus and mitochondrion. Translocates to the mitochondrion and subsequently to the nucleus in response to oxidative stress and exerts an increased cytoprotective effect against oxidative damage. Detected in tau inclusions in brains from neurodegenerative disease patients. Membrane raft localization in astrocytes and neuronal cells requires palmitoylation.

GO - Cellular componenti

  1. chromatin Source: ParkinsonsUK-UCL
  2. cytoplasm Source: UniProtKB
  3. cytosol Source: UniProtKB
  4. extracellular vesicular exosome Source: UniProtKB
  5. mitochondrion Source: UniProtKB
  6. nucleus Source: UniProtKB
  7. plasma membrane Source: UniProtKB-KW
  8. PML body Source: ParkinsonsUK-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Mitochondrion, Nucleus

Pathology & Biotechi

Involvement in diseasei

Parkinson disease 7 (PARK7) [MIM:606324]: A neurodegenerative disorder characterized by resting tremor, postural tremor, bradykinesia, muscular rigidity, anxiety and psychotic episodes. PARK7 has onset before 40 years, slow progression and initial good response to levodopa. Some patients may show traits reminiscent of amyotrophic lateral sclerosis-parkinsonism/dementia complex (Guam disease).4 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti26 – 261M → I in PARK7; does not affect protein stability and degradation; does not interfere with homodimerization. 1 Publication
VAR_020492
Natural varianti64 – 641E → D in PARK7; no apparent effect on protein stability; impaired mitochondrial morphology. 2 Publications
VAR_020493
Natural varianti104 – 1041A → T in PARK7. 1 Publication
VAR_020495
Natural varianti149 – 1491D → A in PARK7. 1 Publication
Corresponds to variant rs74315352 [ dbSNP | Ensembl ].
VAR_020496
Natural varianti166 – 1661L → P in PARK7; reduces protein stability and leads to increased degradation; interferes with homodimerization; abolishes interaction with PIAS2; strongly reduces chaperone activity; ubiquitinated by PARK2, leading to its recognition by HDAC6 and targeting to aggresome where is degraded. 1 Publication
Corresponds to variant rs28938172 [ dbSNP | Ensembl ].
VAR_020498

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi46 – 461C → A: Reduced localization in lipid rafts; when associated with A-106. 4 Publications
Mutagenesisi46 – 461C → A: Reduces protein stability. No effect on oxidation. 4 Publications
Mutagenesisi46 – 461C → S: No effect on mitochondrial translocation. 4 Publications
Mutagenesisi51 – 511V → A: Disrupts dimer formation and strongly reduces ability to eliminate hydrogen peroxide. 1 Publication
Mutagenesisi53 – 531C → A: Strongly reduces chaperone activity and ability to eliminate hydrogen peroxide. 4 Publications
Mutagenesisi53 – 531C → S: No effect on mitochondrial translocation. 4 Publications
Mutagenesisi106 – 1061C → A: Abolishes oxidation, association with mitochondria and protease activity. No effect on chaperone activity. Reduced binding to OTUD7B. 7 Publications
Mutagenesisi106 – 1061C → A: Reduced localization in lipid rafts; when associated with A-46. 7 Publications
Mutagenesisi106 – 1061C → D: Abolishes oxidation and association with mitochondria. No effect on chaperone activity. 7 Publications
Mutagenesisi106 – 1061C → S: No effect on mitochondrial translocation. Reduced protease activity. 7 Publications
Mutagenesisi126 – 1261H → A: Abolishes protease activity. 1 Publication
Mutagenesisi130 – 1301K → R: Partially compensates for loss of stability; when associated with P-166. 1 Publication
Mutagenesisi166 – 1661L → P: Reduced localization in lipid rafts. 1 Publication

Keywords - Diseasei

Disease mutation, Neurodegeneration, Parkinson disease, Parkinsonism, Tumor suppressor

Organism-specific databases

MIMi168600. phenotype.
606324. phenotype.
Orphaneti90020. Amyotrophic lateral sclerosis-parkinsonism-dementia complex.
2828. Young adult-onset Parkinsonism.
PharmGKBiPA32946.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei? – 189Removed in mature formPRO_0000405558
Chaini1 – ?Protein DJ-1PRO_0000157849

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi46 – 461S-palmitoyl cysteine1 Publication
Lipidationi53 – 531S-palmitoyl cysteine1 Publication
Modified residuei67 – 671Phosphotyrosine1 Publication
Modified residuei106 – 1061Cysteine sulfinic acid (-SO2H); alternate1 Publication
Lipidationi106 – 1061S-palmitoyl cysteine; alternate1 Publication
Cross-linki130 – 130Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
Modified residuei148 – 1481N6-acetyllysineBy similarity
Modified residuei182 – 1821N6-succinyllysineBy similarity

Post-translational modificationi

Sumoylated on Lys-130 by PIAS2 or PIAS4; which is enhanced after ultraviolet irradiation and essential for cell-growth promoting activity and transforming activity.1 Publication
Cys-106 is easily oxidized to sulfinic acid.1 Publication
Undergoes cleavage of a C-terminal peptide and subsequent activation of protease activity in response to oxidative stress.

Keywords - PTMi

Acetylation, Isopeptide bond, Lipoprotein, Oxidation, Palmitate, Phosphoprotein, Ubl conjugation, Zymogen

Proteomic databases

MaxQBiQ99497.
PaxDbiQ99497.
PeptideAtlasiQ99497.
PRIDEiQ99497.

2D gel databases

OGPiQ99497.
REPRODUCTION-2DPAGEIPI00298547.
UCD-2DPAGEO14805.
Q99497.

PTM databases

PhosphoSiteiQ99497.

Miscellaneous databases

PMAP-CutDBQ99497.

Expressioni

Tissue specificityi

Highly expressed in pancreas, kidney, skeletal muscle, liver, testis and heart. Detected at slightly lower levels in placenta and brain. Detected in astrocytes, Sertoli cells, spermatogonia, spermatids and spermatozoa.4 Publications

Inductioni

By hydrogen peroxide and UV irradiation.2 Publications

Gene expression databases

BgeeiQ99497.
CleanExiHS_PARK7.
ExpressionAtlasiQ99497. baseline and differential.
GenevestigatoriQ99497.

Organism-specific databases

HPAiCAB005870.
HPA004190.

Interactioni

Subunit structurei

Homodimer. Binds EFCAB6/DJBP and PIAS2. Part of a ternary complex containing PARK7, EFCAB6/DJBP and AR. Interacts (via N-terminus) with OTUD7B. Interacts with BBS1, HIPK1, CLCF1 and MTERF.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-1164361,EBI-1164361
ARP102756EBI-1164361,EBI-608057
DAXXQ9UER73EBI-1164361,EBI-77321
FADDQ131589EBI-1164361,EBI-494804
GNB2L1P632444EBI-1164361,EBI-296739
MTA2O947763EBI-1164361,EBI-1783035
OTUD7BQ6GQQ93EBI-1164361,EBI-527784

Protein-protein interaction databases

BioGridi116446. 62 interactions.
DIPiDIP-35515N.
IntActiQ99497. 36 interactions.
MINTiMINT-5003468.
STRINGi9606.ENSP00000340278.

Structurei

Secondary structure

1
189
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 106Combined sources
Helixi16 – 2813Combined sources
Beta strandi32 – 376Combined sources
Turni38 – 414Combined sources
Beta strandi47 – 493Combined sources
Beta strandi51 – 533Combined sources
Beta strandi55 – 573Combined sources
Helixi58 – 625Combined sources
Beta strandi68 – 725Combined sources
Helixi76 – 849Combined sources
Helixi86 – 9712Combined sources
Beta strandi101 – 1055Combined sources
Turni106 – 1083Combined sources
Helixi109 – 1146Combined sources
Helixi127 – 1293Combined sources
Helixi130 – 1334Combined sources
Turni134 – 1363Combined sources
Beta strandi139 – 1413Combined sources
Beta strandi145 – 1495Combined sources
Beta strandi152 – 1554Combined sources
Helixi158 – 1603Combined sources
Helixi161 – 17313Combined sources
Helixi175 – 1828Combined sources
Helixi183 – 1853Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1J42X-ray2.50A1-189[»]
1P5FX-ray1.10A1-189[»]
1PDVX-ray1.80A1-189[»]
1PDWX-ray2.20A/B/C/D/E/F/G/H1-189[»]
1PE0X-ray1.70A/B1-189[»]
1Q2UX-ray1.60A1-189[»]
1SOAX-ray1.20A1-189[»]
1UCFX-ray1.95A/B1-189[»]
2OR3X-ray1.20A/B1-189[»]
2R1TX-ray1.70A/B2-188[»]
2R1UX-ray1.50A/B2-188[»]
2R1VX-ray1.70A/B2-188[»]
2RK3X-ray1.05A1-189[»]
2RK4X-ray1.15A1-189[»]
2RK6X-ray1.15A1-189[»]
3B36X-ray1.50A1-189[»]
3B38X-ray1.85A1-189[»]
3B3AX-ray1.50A1-189[»]
3BWEX-ray2.40A/B/C/D/E/F/G1-189[»]
3CY6X-ray1.35A1-189[»]
3CYFX-ray1.60A1-189[»]
3CZ9X-ray1.15A1-189[»]
3CZAX-ray1.20A1-189[»]
3EZGX-ray1.15A1-189[»]
3F71X-ray1.20A1-189[»]
3SF8X-ray1.56A/B1-189[»]
4BTEX-ray1.38A1-189[»]
4MNTX-ray1.58A1-189[»]
4MTCX-ray1.47A1-189[»]
4N0MX-ray1.95A1-189[»]
4N12X-ray1.48A1-189[»]
4OQ4X-ray1.49A1-189[»]
4P2GX-ray1.35A1-189[»]
4P34X-ray1.55A1-189[»]
4P35X-ray1.75A1-189[»]
4P36X-ray1.18A1-189[»]
ProteinModelPortaliQ99497.
SMRiQ99497. Positions 3-188.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ99497.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase C56 family.Curated

Phylogenomic databases

eggNOGiCOG0693.
HOGENOMiHOG000063194.
HOVERGENiHBG053511.
InParanoidiQ99497.
KOiK05687.
OMAiGTTFPFA.
OrthoDBiEOG7CVPZX.
PhylomeDBiQ99497.
TreeFamiTF300119.

Family and domain databases

Gene3Di3.40.50.880. 1 hit.
InterProiIPR029062. Class_I_gatase-like.
IPR006287. DJ1.
IPR002818. ThiJ/PfpI.
[Graphical view]
PfamiPF01965. DJ-1_PfpI. 1 hit.
[Graphical view]
SUPFAMiSSF52317. SSF52317. 1 hit.
TIGRFAMsiTIGR01383. not_thiJ. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q99497-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MASKRALVIL AKGAEEMETV IPVDVMRRAG IKVTVAGLAG KDPVQCSRDV
60 70 80 90 100
VICPDASLED AKKEGPYDVV VLPGGNLGAQ NLSESAAVKE ILKEQENRKG
110 120 130 140 150
LIAAICAGPT ALLAHEIGFG SKVTTHPLAK DKMMNGGHYT YSENRVEKDG
160 170 180
LILTSRGPGT SFEFALAIVE ALNGKEVAAQ VKAPLVLKD
Length:189
Mass (Da):19,891
Last modified:July 5, 2004 - v2
Checksum:i4B21661B3A76BC67
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti119 – 1191F → C in BAB71782. 1 PublicationCurated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti26 – 261M → I in PARK7; does not affect protein stability and degradation; does not interfere with homodimerization. 1 Publication
VAR_020492
Natural varianti64 – 641E → D in PARK7; no apparent effect on protein stability; impaired mitochondrial morphology. 2 Publications
VAR_020493
Natural varianti98 – 981R → Q.4 Publications
Corresponds to variant rs71653619 [ dbSNP | Ensembl ].
VAR_020494
Natural varianti104 – 1041A → T in PARK7. 1 Publication
VAR_020495
Natural varianti149 – 1491D → A in PARK7. 1 Publication
Corresponds to variant rs74315352 [ dbSNP | Ensembl ].
VAR_020496
Natural varianti150 – 1501G → S.1 Publication
VAR_020497
Natural varianti163 – 1631E → K.1 Publication
VAR_034801
Natural varianti166 – 1661L → P in PARK7; reduces protein stability and leads to increased degradation; interferes with homodimerization; abolishes interaction with PIAS2; strongly reduces chaperone activity; ubiquitinated by PARK2, leading to its recognition by HDAC6 and targeting to aggresome where is degraded. 1 Publication
Corresponds to variant rs28938172 [ dbSNP | Ensembl ].
VAR_020498
Natural varianti171 – 1711A → S.1 Publication
VAR_020499

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D61380 mRNA. Translation: BAA09603.2.
AF021819 mRNA. Translation: AAC12806.1.
AB073864 mRNA. Translation: BAB71782.1.
AK312000 mRNA. Translation: BAG34938.1.
AL034417 Genomic DNA. Translation: CAB52550.1.
CH471130 Genomic DNA. Translation: EAW71591.1.
BC008188 mRNA. Translation: AAH08188.1.
AB045294 Genomic DNA. No translation available.
AY648999 Genomic DNA. Translation: AAT68961.1.
CCDSiCCDS93.1.
PIRiJC5394.
RefSeqiNP_001116849.1. NM_001123377.1.
NP_009193.2. NM_007262.4.
XP_005263481.1. XM_005263424.1.
UniGeneiHs.419640.

Genome annotation databases

EnsembliENST00000338639; ENSP00000340278; ENSG00000116288.
ENST00000377488; ENSP00000366708; ENSG00000116288.
ENST00000377491; ENSP00000366711; ENSG00000116288.
ENST00000493373; ENSP00000465404; ENSG00000116288.
ENST00000493678; ENSP00000418770; ENSG00000116288.
GeneIDi11315.
KEGGihsa:11315.
UCSCiuc001aou.4. human.

Polymorphism databases

DMDMi56404943.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

SHMPD

The Singapore human mutation and polymorphism database

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D61380 mRNA. Translation: BAA09603.2 .
AF021819 mRNA. Translation: AAC12806.1 .
AB073864 mRNA. Translation: BAB71782.1 .
AK312000 mRNA. Translation: BAG34938.1 .
AL034417 Genomic DNA. Translation: CAB52550.1 .
CH471130 Genomic DNA. Translation: EAW71591.1 .
BC008188 mRNA. Translation: AAH08188.1 .
AB045294 Genomic DNA. No translation available.
AY648999 Genomic DNA. Translation: AAT68961.1 .
CCDSi CCDS93.1.
PIRi JC5394.
RefSeqi NP_001116849.1. NM_001123377.1.
NP_009193.2. NM_007262.4.
XP_005263481.1. XM_005263424.1.
UniGenei Hs.419640.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1J42 X-ray 2.50 A 1-189 [» ]
1P5F X-ray 1.10 A 1-189 [» ]
1PDV X-ray 1.80 A 1-189 [» ]
1PDW X-ray 2.20 A/B/C/D/E/F/G/H 1-189 [» ]
1PE0 X-ray 1.70 A/B 1-189 [» ]
1Q2U X-ray 1.60 A 1-189 [» ]
1SOA X-ray 1.20 A 1-189 [» ]
1UCF X-ray 1.95 A/B 1-189 [» ]
2OR3 X-ray 1.20 A/B 1-189 [» ]
2R1T X-ray 1.70 A/B 2-188 [» ]
2R1U X-ray 1.50 A/B 2-188 [» ]
2R1V X-ray 1.70 A/B 2-188 [» ]
2RK3 X-ray 1.05 A 1-189 [» ]
2RK4 X-ray 1.15 A 1-189 [» ]
2RK6 X-ray 1.15 A 1-189 [» ]
3B36 X-ray 1.50 A 1-189 [» ]
3B38 X-ray 1.85 A 1-189 [» ]
3B3A X-ray 1.50 A 1-189 [» ]
3BWE X-ray 2.40 A/B/C/D/E/F/G 1-189 [» ]
3CY6 X-ray 1.35 A 1-189 [» ]
3CYF X-ray 1.60 A 1-189 [» ]
3CZ9 X-ray 1.15 A 1-189 [» ]
3CZA X-ray 1.20 A 1-189 [» ]
3EZG X-ray 1.15 A 1-189 [» ]
3F71 X-ray 1.20 A 1-189 [» ]
3SF8 X-ray 1.56 A/B 1-189 [» ]
4BTE X-ray 1.38 A 1-189 [» ]
4MNT X-ray 1.58 A 1-189 [» ]
4MTC X-ray 1.47 A 1-189 [» ]
4N0M X-ray 1.95 A 1-189 [» ]
4N12 X-ray 1.48 A 1-189 [» ]
4OQ4 X-ray 1.49 A 1-189 [» ]
4P2G X-ray 1.35 A 1-189 [» ]
4P34 X-ray 1.55 A 1-189 [» ]
4P35 X-ray 1.75 A 1-189 [» ]
4P36 X-ray 1.18 A 1-189 [» ]
ProteinModelPortali Q99497.
SMRi Q99497. Positions 3-188.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116446. 62 interactions.
DIPi DIP-35515N.
IntActi Q99497. 36 interactions.
MINTi MINT-5003468.
STRINGi 9606.ENSP00000340278.

Protein family/group databases

MEROPSi C56.002.

PTM databases

PhosphoSitei Q99497.

Polymorphism databases

DMDMi 56404943.

2D gel databases

OGPi Q99497.
REPRODUCTION-2DPAGE IPI00298547.
UCD-2DPAGE O14805.
Q99497.

Proteomic databases

MaxQBi Q99497.
PaxDbi Q99497.
PeptideAtlasi Q99497.
PRIDEi Q99497.

Protocols and materials databases

DNASUi 11315.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000338639 ; ENSP00000340278 ; ENSG00000116288 .
ENST00000377488 ; ENSP00000366708 ; ENSG00000116288 .
ENST00000377491 ; ENSP00000366711 ; ENSG00000116288 .
ENST00000493373 ; ENSP00000465404 ; ENSG00000116288 .
ENST00000493678 ; ENSP00000418770 ; ENSG00000116288 .
GeneIDi 11315.
KEGGi hsa:11315.
UCSCi uc001aou.4. human.

Organism-specific databases

CTDi 11315.
GeneCardsi GC01P008014.
GeneReviewsi PARK7.
HGNCi HGNC:16369. PARK7.
HPAi CAB005870.
HPA004190.
MIMi 168600. phenotype.
602533. gene.
606324. phenotype.
neXtProti NX_Q99497.
Orphaneti 90020. Amyotrophic lateral sclerosis-parkinsonism-dementia complex.
2828. Young adult-onset Parkinsonism.
PharmGKBi PA32946.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0693.
HOGENOMi HOG000063194.
HOVERGENi HBG053511.
InParanoidi Q99497.
KOi K05687.
OMAi GTTFPFA.
OrthoDBi EOG7CVPZX.
PhylomeDBi Q99497.
TreeFami TF300119.

Enzyme and pathway databases

SignaLinki Q99497.

Miscellaneous databases

ChiTaRSi PARK7. human.
EvolutionaryTracei Q99497.
GeneWikii PARK7.
GenomeRNAii 11315.
NextBioi 42983.
PMAP-CutDB Q99497.
PROi Q99497.
SOURCEi Search...

Gene expression databases

Bgeei Q99497.
CleanExi HS_PARK7.
ExpressionAtlasi Q99497. baseline and differential.
Genevestigatori Q99497.

Family and domain databases

Gene3Di 3.40.50.880. 1 hit.
InterProi IPR029062. Class_I_gatase-like.
IPR006287. DJ1.
IPR002818. ThiJ/PfpI.
[Graphical view ]
Pfami PF01965. DJ-1_PfpI. 1 hit.
[Graphical view ]
SUPFAMi SSF52317. SSF52317. 1 hit.
TIGRFAMsi TIGR01383. not_thiJ. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "DJ-1, a novel oncogene which transforms mouse NIH3T3 cells in cooperation with ras."
    Nagakubo D., Taita T., Kitaura H., Ikeda M., Tamai K., Iguchi-Ariga S.M.M., Ariga H.
    Biochem. Biophys. Res. Commun. 231:509-513(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Tissue: Cervix carcinoma.
  2. "Homo sapiens RNA-binding protein regulatory subunit mRNA."
    Beaudoin R., Hod Y.
    Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Lung.
  3. "Human DJ-1 cDNA from PC3 cells."
    Ariga H., Niki T.
    Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Thalamus.
  5. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Cervix.
  8. "Molecular cloning of human and mouse DJ-1 genes and identification of Sp1-dependent activation of the human DJ-1 promoter."
    Taira T., Takahashi K., Kitagawa R., Iguchi-Ariga S.M.M., Ariga H.
    Gene 263:285-292(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-6.
    Tissue: Kidney.
  9. Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 6-27; 33-89; 99-122 AND 149-175, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
  10. "DJ-1 gene G150S mutation."
    Zou H.Q., Chan P.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 138-189, VARIANT SER-150.
  11. "DJ-1 positively regulates the androgen receptor by impairing the binding of PIASx alpha to the receptor."
    Takahashi K., Taira T., Niki T., Seino C., Iguchi-Ariga S.M.M., Ariga H.
    J. Biol. Chem. 276:37556-37563(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PIAS2, SUBCELLULAR LOCATION, FUNCTION.
  12. "L166P mutant DJ-1, causative for recessive Parkinson's disease, is degraded through the ubiquitin-proteasome system."
    Miller D.W., Ahmad R., Hague S., Baptista M.J., Canet-Aviles R., McLendon C., Carter D.M., Zhu P.-P., Stadler J., Chandran J., Klinefelter G.R., Blackstone C., Cookson M.R.
    J. Biol. Chem. 278:36588-36595(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEGRADATION BY THE PROTEASOME, SUBCELLULAR LOCATION, INTERACTION WITH PIAS2, HOMODIMERIZATION, MUTAGENESIS OF LYS-130, CHARACTERIZATION OF VARIANT PARK7 PRO-166.
  13. "A missense mutation (L166P) in DJ-1, linked to familial Parkinson's disease, confers reduced protein stability and impairs homo-oligomerization."
    Moore D.J., Zhang L., Dawson T.M., Dawson V.L.
    J. Neurochem. 87:1558-1567(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEGRADATION BY THE PROTEASOME, CHARACTERIZATION OF VARIANTS PARK7 ILE-26 AND PRO-166.
  14. "DJBP: a novel DJ-1-binding protein, negatively regulates the androgen receptor by recruiting histone deacetylase complex, and DJ-1 antagonizes this inhibition by abrogation of this complex."
    Niki T., Takahashi-Niki K., Taira T., Iguchi-Ariga S.M.M., Ariga H.
    Mol. Cancer Res. 1:247-261(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH EFCAB6, FUNCTION.
  15. "Immunocytochemical localization of DJ-1 in human male reproductive tissue."
    Yoshida K., Sato Y., Yoshiike M., Nozawa S., Ariga H., Iwamoto T.
    Mol. Reprod. Dev. 66:391-397(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
  16. Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
  17. Cited for: TISSUE SPECIFICITY.
  18. "DJ-1 has a role in antioxidative stress to prevent cell death."
    Taira T., Saito Y., Niki T., Iguchi-Ariga S.M., Takahashi K., Ariga H.
    EMBO Rep. 5:213-218(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION, MUTAGENESIS OF VAL-51 AND CYS-53.
  19. "DJ-1 is a redox-dependent molecular chaperone that inhibits alpha-synuclein aggregate formation."
    Shendelman S., Jonason A., Martinat C., Leete T., Abeliovich A.
    PLoS Biol. 2:1-10(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF CYS-46; CYS-53 AND CYS-106.
  20. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
    Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
    Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-67, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. "Proper SUMO-1 conjugation is essential to DJ-1 to exert its full activities."
    Shinbo Y., Niki T., Taira T., Ooe H., Takahashi-Niki K., Maita C., Seino C., Iguchi-Ariga S.M.M., Ariga H.
    Cell Death Differ. 13:96-108(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION AT LYS-130, OXIDATION, SUBCELLULAR LOCATION, INDUCTION, FUNCTION.
  22. "DJ-1 interacts with HIPK1 and affects H2O2-induced cell death."
    Sekito A., Koide-Yoshida S., Niki T., Taira T., Iguchi-Ariga S.M.M., Ariga H.
    Free Radic. Res. 40:155-165(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH HIPK1, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-106.
  23. "DJ-1, a cancer- and Parkinson's disease-associated protein, stabilizes the antioxidant transcriptional master regulator Nrf2."
    Clements C.M., McNally R.S., Conti B.J., Mak T.W., Ting J.P.
    Proc. Natl. Acad. Sci. U.S.A. 103:15091-15096(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  24. Cited for: FUNCTION.
  25. "Mitochondrial localization of DJ-1 leads to enhanced neuroprotection."
    Junn E., Jang W.H., Zhao X., Jeong B.S., Mouradian M.M.
    J. Neurosci. Res. 87:123-129(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-46; CYS-53 AND CYS-106.
  26. "Parkinson disease protein DJ-1 converts from a zymogen to a protease by carboxyl-terminal cleavage."
    Chen J., Li L., Chin L.S.
    Hum. Mol. Genet. 19:2395-2408(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVE SITES, MUTAGENESIS OF CYS-106 AND HIS-126.
  27. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  28. "DJ-1 enhances cell survival through the binding of cezanne, a negative regulator of NF-{kappa}B."
    McNally R.S., Davis B.K., Clements C.M., Accavitti-Loper M.A., Mak T.W., Ting J.P.
    J. Biol. Chem. 286:4098-4106(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH BBS1; CLCF1; MTERF AND OTUD7B, MUTAGENESIS OF CYS-106.
  29. "DJ-1 associates with lipid rafts by palmitoylation and regulates lipid rafts-dependent endocytosis in astrocytes."
    Kim K.S., Kim J.S., Park J.Y., Suh Y.H., Jou I., Joe E.H., Park S.M.
    Hum. Mol. Genet. 22:4805-4817(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PALMITOYLATION AT CYS-46; CYS-53 AND CYS-106, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-46; CYS-106 AND LEU-166.
  30. "Crystal structure of DJ-1/RS and implication on familial Parkinson's disease."
    Huai Q., Sun Y., Wang H., Chin L.-S., Li L., Robinson H., Ke H.
    FEBS Lett. 549:171-175(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS), HOMODIMERIZATION.
  31. "Crystal structure of human DJ-1, a protein associated with early onset Parkinson's disease."
    Tao X., Tong L.
    J. Biol. Chem. 278:31372-31379(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF WILD-TYPE AND MUTANT ARG-130, HOMODIMERIZATION.
  32. "The crystal structure of DJ-1, a protein related to male fertility and Parkinson's disease."
    Honbou K., Suzuki N.N., Horiuchi M., Niki T., Taira T., Ariga H., Inagaki F.
    J. Biol. Chem. 278:31380-31384(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS), HOMODIMERIZATION.
  33. "Crystal structures of human DJ-1 and Escherichia coli Hsp31, which share an evolutionarily conserved domain."
    Lee S.-J., Kim S.J., Kim I.-K., Ko J., Jeong C.-S., Kim G.-H., Park C., Kang S.-O., Suh P.-G., Lee H.-S., Cha S.-S.
    J. Biol. Chem. 278:44552-44559(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), FUNCTION, OXIDATION AT CYS-106, HOMODIMERIZATION.
  34. "The 1.1-A resolution crystal structure of DJ-1, the protein mutated in autosomal recessive early onset Parkinson's disease."
    Wilson M.A., Collins J.L., Hod Y., Ringe D., Petsko G.A.
    Proc. Natl. Acad. Sci. U.S.A. 100:9256-9261(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.1 ANGSTROMS), HOMODIMERIZATION, OXIDATION, LACK OF PROTEOLYTIC ACTIVITY.
  35. "The Parkinson's disease protein DJ-1 is neuroprotective due to cysteine-sulfinic acid-driven mitochondrial localization."
    Canet-Aviles R.M., Wilson M.A., Miller D.W., Ahmad R., McLendon C., Bandyopadhyay S., Baptista M.J., Ringe D., Petsko G.A., Cookson M.R.
    Proc. Natl. Acad. Sci. U.S.A. 101:9103-9108(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS), MUTAGENESIS OF CYS-46; CYS-53 AND CYS-106, OXIDATION, FUNCTION, SUBCELLULAR LOCATION.
  36. "The role of pathogenic DJ-1 mutations in Parkinson's disease."
    Abou-Sleiman P.M., Healy D.G., Quinn N., Lees A.J., Wood N.W.
    Ann. Neurol. 54:283-286(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS PARK7 ILE-26 AND ALA-149, VARIANT GLN-98.
  37. Cited for: VARIANT PARK7 PRO-166, SUBCELLULAR LOCATION.
  38. Cited for: VARIANT GLN-98.
  39. Cited for: VARIANT PARK7 ASP-64, X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
  40. "Differential effects of Parkinson's disease-associated mutations on stability and folding of DJ-1."
    Goerner K., Holtorf E., Odoy S., Nuscher B., Yamamoto A., Regula J.T., Beyer K., Haass C., Kahle P.J.
    J. Biol. Chem. 279:6943-6951(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF VARIANTS PARK7 ASP-64 AND PRO-166.
  41. Cited for: VARIANT PARK7 THR-104, VARIANTS GLN-98 AND SER-171.
  42. Cited for: VARIANT GLN-98.
  43. Cited for: VARIANT LYS-163.
  44. "Parkin-mediated K63-linked polyubiquitination targets misfolded DJ-1 to aggresomes via binding to HDAC6."
    Olzmann J.A., Li L., Chudaev M.V., Chen J., Perez F.A., Palmiter R.D., Chin L.S.
    J. Cell Biol. 178:1025-1038(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF VARIANT PARK7 PRO-166.
  45. "Reduced basal autophagy and impaired mitochondrial dynamics due to loss of Parkinson's disease-associated protein DJ-1."
    Krebiehl G., Ruckerbauer S., Burbulla L.F., Kieper N., Maurer B., Waak J., Wolburg H., Gizatullina Z., Gellerich F.N., Woitalla D., Riess O., Kahle P.J., Proikas-Cezanne T., Kruger R.
    PLoS ONE 5:E9367-E9367(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT ASP-64.

Entry informationi

Entry nameiPARK7_HUMAN
AccessioniPrimary (citable) accession number: Q99497
Secondary accession number(s): B2R4Z1
, O14805, Q6DR95, Q7LFU2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 7, 2004
Last sequence update: July 5, 2004
Last modified: November 26, 2014
This is version 150 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Peptidase families
    Classification of peptidase families and list of entries
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3